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Database: UniProt
Entry: A0A0M2XKN4_9CORY
LinkDB: A0A0M2XKN4_9CORY
Original site: A0A0M2XKN4_9CORY 
ID   A0A0M2XKN4_9CORY        Unreviewed;       411 AA.
AC   A0A0M2XKN4;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:NMF09422.1};
GN   ORFNames=HF852_07420 {ECO:0000313|EMBL:NMF09422.1};
OS   Corynebacterium xerosis.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1725 {ECO:0000313|EMBL:NMF09422.1, ECO:0000313|Proteomes:UP000589552};
RN   [1] {ECO:0000313|EMBL:NMF09422.1, ECO:0000313|Proteomes:UP000589552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BL-383-APC-2I {ECO:0000313|EMBL:NMF09422.1,
RC   ECO:0000313|Proteomes:UP000589552};
RA   Hitch T.C.A., Wylensek D., Clavel T.;
RL   Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU362125};
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:NMF09422.1}.
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DR   EMBL; JABAGA010000004; NMF09422.1; -; Genomic_DNA.
DR   RefSeq; WP_046650344.1; NZ_LAYS01000029.1.
DR   AlphaFoldDB; A0A0M2XKN4; -.
DR   OrthoDB; 8876745at2; -.
DR   Proteomes; UP000589552; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR   Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR   Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR   Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR   InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR   InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR   InterPro; IPR036250; AcylCo_DH-like_C.
DR   InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR   InterPro; IPR013786; AcylCoA_DH/ox_N.
DR   InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR   PANTHER; PTHR48083:SF13; ACYL-COA DEHYDROGENASE FAMILY MEMBER 11; 1.
DR   PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362125};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU362125};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362125}.
FT   DOMAIN          7..130
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          134..234
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          246..395
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   411 AA;  45722 MW;  7DE76478C2CC3A3D CRC64;
     MDFRESDRAR EYRERLEAFM DECVYPAEAT IAEQVRASGD PHHHPAAMEE LKAEAKSRGL
     WNLFHPHPGR GPGLSNVEYA PLAEIMGRSP HIAPEACNCN APDTGNMEVL ELYGTEEHRR
     RWLEPLLAGE IRSAFCMTEP GVASSDATNV AMRMERVDGG WKLNGRKWFT SNGMHPNLRV
     LIVMGKTSPD AETHRQQSML VVPADAPGVT VLRDLPVFGF HDREGHAEVL FDDVVVPDFD
     VLKGEGEGFR IAQDRLGPGR IHHCMRAIGM AERALEMMCR RALERSTFGT LLADRDNVRD
     RIAQARIDIE MARLLTLKAA WLMDEAGNKA ARQEIAAIKV AAPATALRVV DQAIQLFGGE
     GVTDDVPLAQ FWAGLRALRL ADGPDEVHLM TIARGELRRY RGDRTPKGGE R
//
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